5MCX

The structure of the mature HIV-1 CA hexamer in intact virus particles

5MCX の概要

• エントリーDOI: 10.2210/pdb5mcx/pdb
• EMDBエントリー: 3465
• 分子名称: Capsid protein p24 (1 entity in total)
• 機能のキーワード: retrovirus, hiv-1, capsid, hexamer, viral protein
• 由来する生物種: Human immunodeficiency virus 1
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 591702.43

構造登録者

Mattei, S.,Glass, B.,Hagen, W.J.H.,Kraeusslich, H.-G.,Briggs, J.A.G. (登録日: 2016-11-10, 公開日: 2016-12-28, 最終更新日: 2024-05-15)

主引用文献

Mattei, S.,Glass, B.,Hagen, W.J.,Krausslich, H.G.,Briggs, J.A.
The structure and flexibility of conical HIV-1 capsids determined within intact virions.
Science, 354:1434-1437, 2016

PubMed Abstract: HIV-1 contains a cone-shaped capsid encasing the viral genome. This capsid is thought to follow fullerene geometry-a curved hexameric lattice of the capsid protein, CA, closed by incorporating 12 CA pentamers. Current models for core structure are based on crystallography of hexameric and cross-linked pentameric CA, electron microscopy of tubular CA arrays, and simulations. Here, we report subnanometer-resolution cryo-electron tomography structures of hexameric and pentameric CA within intact HIV-1 particles. Whereas the hexamer structure is compatible with crystallography studies, the pentamer forms using different interfaces. Determining multiple structures revealed how CA flexes to form the variably curved core shell. We show that HIV-1 CA assembles both aberrant and perfect fullerene cones, supporting models in which conical cores assemble de novo after maturation.

PubMed: 27980210
DOI: 10.1126/science.aah4972

実験手法

ELECTRON MICROSCOPY (6.8 Å)